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. Author manuscript; available in PMC: 2018 Aug 19.
Published in final edited form as: Nat Struct Mol Biol. 2018 Feb 19;25(3):217–224. doi: 10.1038/s41594-018-0031-y

Figure 1. The crystal structure of human GPT in complex with tunicamycin reveals the structural basis for high affinity binding.

Figure 1

a, hGPT crystallized as a homodimer with one tunicamycin molecule (magenta sticks) bound to the cytosolic active site cavity of each protomer, tightly enclosed by loops A and E. The two protomers are related by pseudo-twofold rotational symmetry and are covalently linked by a disulfide bond between TM3 of each protomer. b, Cartoon representation of the cytoplasmic view, rainbow colored from N-terminus (blue) to C-terminus (red). c, Representative ITC raw data (top) and binding isotherm (bottom) for tunicamycin interacting with wild-type hGPT; Kd = 4.3 nM, ΔH° = −10.8 kcal/mol. This ITC experiment was performed in triplicate (technical replicates (5.6+/−1.3 nM, mean +/− S.E.M.)).